5GW8

Crystal structure of a putative DAG-like lipase (MgMDL2) from Malassezia globosa

Summary for 5GW8

• Entry DOI: 10.2210/pdb5gw8/pdb
• Descriptor: Hypothetical secretory lipase (Family 3), 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (8 entities in total)
• Functional Keywords: dag-like lipase, n-linked glycosylation, hydrolase
• Biological source: Malassezia globosa (strain ATCC MYA-4612 / CBS 7966) (Dandruff-associated fungus)
• Total number of polymer chains: 2
• Total formula weight: 65577.01

Authors

Xu, J.,Xu, H.,Liu, J. (deposition date: 2016-09-09, release date: 2017-09-27, Last modification date: 2024-11-13)

Primary citation

Lan, D.,Xu, H.,Xu, J.,Dubin, G.,Liu, J.,Iqbal Khan, F.,Wang, Y.
Malassezia globosa MgMDL2 lipase: Crystal structure and rational modification of substrate specificity.
Biochem. Biophys. Res. Commun., 488:259-265, 2017

PubMed Abstract: Lipases play an important role in physiological metabolism and diseases, and also have multiple industrial applications. Rational modification of lipase specificity may increase the commercial utility of this group of enzymes, but is hindered by insufficient mechanistic understanding. Here, we report the 2.0 Å resolution crystal structure of a mono- and di-acylglycerols lipase from Malassezia globosa (MgMDL2). Interestingly, residues Phe278 and Glu282 were found to involve in substrate recognition because mutation on each residue led to convert MgMDL2 to a triacylglycerol (TAG) lipase. The Phe278Ala and Glu282Ala mutants also acquired ability to synthesize TAGs by esterification of glycerol and fatty acids. By in silicon analysis, steric hindrance of these residues seemed to be key factors for the altered substrate specificity. Our work may shed light on understanding the unique substrate selectivity mechanism of mono- and di-acylglycerols lipases, and provide a new insight for engineering biocatalysts with desired catalytic behaviors for biotechnological application.

PubMed: 28433636
DOI: 10.1016/j.bbrc.2017.04.103

Experimental method

X-RAY DIFFRACTION (2 Å)